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  • Glutamine synthetase  (3)
  • Springer  (3)
  • Wiley
  • 1
    ISSN: 1432-2048
    Keywords: Key words:Arabidopsis (stm mutant) ; Gas exchange ; Gene expression ; Glutamine synthetase ; Mutant (Arabidopsis ; stm) ; Photorespiration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. The regulation by photorespiration of the transcript level corresponding to plastidic glutamine synthetase (GS-2) was investigated in the leaves of Arabidopsis thaliana (L.) Heynh.. Photorespiration was suppressed by growing the plants in an atmosphere containing 300 Pa CO2. Suppression of photorespiration was demonstrated by the ability of the conditionally lethal serine hydroxymethyltransferase (SHMT)-deficient stm mutant of A. thaliana to grow normally under these conditions. In contrast to previous studies with bean or pea that were performed at very high CO2 partial pressure (2–4 kPa; Edwards and Coruzzi, 1989, Plant Cell 1: 241–248; Cock et al., 1991, Plant Mol Biol 17: 761–771), suppression of photorespiration during growth of A. thaliana in an atmosphere with 300 Pa CO2 had no effect on the leaf GS-2 transcript level. In the short term, neither suppression of photorespiration induced by the transfer of air-grown A. thaliana plants into a CO2-enriched atmosphere, nor an increase in the rate of photorespiration achieved by the transfer of high-CO2-grown A. thaliana plants into air resulted in a change in the GS-2 mRNA level. The absence of photorespiratory ammonium release in leaves of the stm mutant had no effect on the GS-2 transcript level. Overall, our data argue against a control by photorespiration of the A. thaliana leaf GS-2 mRNA pool. In contrast, regulation of the leaf SHMT mRNA level may involve a negative feedback effect of at least one metabolite derived from the glycine/serine conversion during photorespiration, as indicated by the overexpression of SHMT transcripts in the leaves of the stm mutant.
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  • 2
    ISSN: 1432-2048
    Keywords: Gene expression ; Glutamine synthetase ; Nitrogen source ; Phosphinothricin ; Phytochrome ; Solanum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The co-action of light and the N-source in the regulation of the expression of the single-copy gene encoding plastidic glutamine synthetase (GS-2) and of the multigene family encoding cytosolic glutamine synthetase (GS-1) was investigated in the cotyledons of tomato (Lycopersicon esculentum L.). Light, acting at red/far red or at blue regions of the spectrum increased the abundance of the GS-2 gene product and induced a modification of GS-2 subunits, resulting in the appearance of two GS-2 proteins exhibiting different molecular weights. The magnitude of the light stimulation of GS-2 gene expression was independent of the nitrogen source. However, following red- or far-red-light treatment of etiolated tomato cotyledons, two GS-2 proteins were found when nitrate was the N-source, while only one GS-2 protein was present with ammonium as the sole nitrogen source. Thus, light of specific wavelengths and N-substrates seem to act in concert to regulate GS-2 subunit composition. Tomato GS-1 gene expression was unaffected by light. Ammonium provided externally increased the level of the tomato GS-1 protein. Irrespective of the N-source or the light quality, the GS-1 subunits were represented by polypeptides of similar molecular weight in tomato cotyledons. However, phosphinothricin-induced inhibition of GS activity resulted in the appearance of at least one additional GS-1 polypeptide in etiolated or in green tomato cotyledons. In addition, impairment of GS activity in green tomato cotyledons by phosphinothricin was correlated with an increased level of the GS-1 transcript. Taken together, our data suggest a metabolic control of GS-1 gene expression in green tomato cotyledons.
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  • 3
    ISSN: 1432-2048
    Keywords: C4-plant ; Cell type specificity ; Glutamatesynthase ; Glutamine synthetase ; Nitrogen metabolism ; Zea (ammonia assimilation)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cellular localization of the enzymes involved in primary nitrogen assimilation was investigated following separation of mesophyll protoplasts and bundle-sheath cells of maize (Zea mays L.) leaves. Determination of the enzymatic activities in the two types of cell revealed that nitrate and nitrite reductase are principally located in the mesophyll cells whereas glutamine synthetase (GS) and ferredoxin-dependent glutamate synthase (Fd-GOGAT) are present in both tissues with a preferential location in the bundle-sheath strands. In order to confirm the results obtained by this conventional biochemical method we have used an in-situ immunofluorescence technique to unambiguously localize GS and Fd-GOGAT at the cellular level. Thin-sectioned maize leaves treated with specific GS and Fd-GOGAT antisera followed by conjugation with fluorescein-isothiocyanate-labelled sheep anti-rabbit immunoglobulins clearly show that GS is equally distributed within the leaf whereas Fd-GOGAT is mostly present in the chloroplasts of the bundle-sheath cells. The cellular localization of nitrate reductase, nitrite reductase, GS-2 and Fd-GOGAT in maize leaf cell types strongly indicates that primary nitrogen assimilation functions in the mesophyll cells while photorespiratory nitrogen recycling is restricted to the bundle-sheath cells.
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